PDB ID:  pdb_00004l28
  • Crystal structure of delta516-525 human cystathionine beta-synthase D444N mutant containing C-terminal 6xHis tag
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.626 Å
  • Deposition date: 2013-06-04
Number of assemblies:  2
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others E (PLPStructure of PLPPLP ), I (PLPStructure of PLPPLP )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 42-548 (2-551)
Mutations (UniProt numbering)
Missing residues 402LEU-402LEU:515GLN-527ARG
Structural gaps Exists
Uniprot ID P35520 →UniprotKB
label_asym_ids of heme F
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 43-549 (2-551)
Mutations (UniProt numbering)
Missing residues 297GLU-297GLU:401ASP-401ASP:403THR-404GLU:515GLN-526GLN
Structural gaps Exists
Uniprot ID P35520 →UniprotKB
label_asym_ids of heme J
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others G (PLPStructure of PLPPLP ), K (PLPStructure of PLPPLP )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 42-550 (2-551)
Mutations (UniProt numbering)
Missing residues 297GLU-297GLU:401ASP-401ASP:403THR-403THR:515GLN-526GLN
Structural gaps Exists
Uniprot ID P35520 →UniprotKB
label_asym_ids of heme H
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 43-549 (2-551)
Mutations (UniProt numbering)
Missing residues 401ASP-401ASP:403THR-403THR:515GLN-526GLN
Structural gaps Exists
Uniprot ID P35520 →UniprotKB
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å